ID D8R2R8_SELML Unreviewed; 2144 AA.
AC D8R2R8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN ORFNames=SELMODRAFT_439142 {ECO:0000313|EMBL:EFJ34117.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ34117.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + L-glutamine +
CC NADH; Xref=Rhea:RHEA:13753, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58359; EC=1.4.1.14;
CC Evidence={ECO:0000256|ARBA:ARBA00024267};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|PIRSR:PIRSR000187-2};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000256|PIRSR:PIRSR000187-2};
CC -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NAD(+)
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00004944}.
CC -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC {ECO:0000256|ARBA:ARBA00004802}.
CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
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DR EMBL; GL377570; EFJ34117.1; -; Genomic_DNA.
DR RefSeq; XP_002965279.1; XM_002965233.1.
DR STRING; 88036.D8R2R8; -.
DR EnsemblPlants; EFJ34117; EFJ34117; SELMODRAFT_439142.
DR Gramene; EFJ34117; EFJ34117; SELMODRAFT_439142.
DR KEGG; smo:SELMODRAFT_439142; -.
DR eggNOG; KOG0399; Eukaryota.
DR HOGENOM; CLU_000422_8_2_1; -.
DR InParanoid; D8R2R8; -.
DR OMA; PHTFFRE; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016040; F:glutamate synthase (NADH) activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019676; P:ammonia assimilation cycle; IBA:GO_Central.
DR GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
DR GO; GO:0097054; P:L-glutamate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd00713; GltS; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 3.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 2.160.20.60; Glutamate synthase, alpha subunit, C-terminal domain; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR InterPro; IPR006982; Glu_synth_centr_N.
DR InterPro; IPR012220; Glu_synth_euk.
DR InterPro; IPR002932; Glu_synthdom.
DR InterPro; IPR006005; Glut_synth_ssu1.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR NCBIfam; TIGR01317; GOGAT_sm_gam; 1.
DR PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF00310; GATase_2; 1.
DR Pfam; PF04898; Glu_syn_central; 1.
DR Pfam; PF01645; Glu_synthase; 2.
DR Pfam; PF01493; GXGXG; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PIRSF; PIRSF000187; GOGAT; 2.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291, ECO:0000256|PIRSR:PIRSR000187-2};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000187-
KW 2}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514}.
FT DOMAIN 111..516
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT ACT_SITE 111
FT /note="For GATase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-1"
FT BINDING 1241
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
SQ SEQUENCE 2144 AA; 234616 MW; B37C4422669420D9 CRC64;
MQACLGLSLN QAAWMHRRAR ATEATALGSI CSSRLSSAVP SLSCATAGLK VLHTSFLPSR
NLDRWGTGSS HLQRWNGERR MYRCVVTMSS MSQVPEGPLG LYDPALDKDS CGVGFVAELS
AKPSRQTVTD ALEMLVRMAH RGACGCETNT GDGAGVLLAL PHDFFASIAK DEIGCELPPP
SEYAVGMFFL PTSETRRMES KNVFNKVAES LGHTVLGWRS VVTDNSDLGK SALATEPVVE
QVFLTGSSRS SASLEQQMYI LRKLSMVAIR AALNLQHGAV RDFYICSLSS RTVVYKGQLK
PDQLKKYYAS DLCHDKFTSY MALVHSRFST NTFPSWDRAQ PMRVLGHNGE INTLRGNVNW
MRAREGLLKC RALDLSNDEL QKLLPIVDAS SSDSGSFDGV LEFLVRSGRS LPEAMMMMIP
EAWQNDKNMD PERRALYEYF SALMEPWDGP ALIAFSDGRY LGATLDRNGL RPGRYYITHS
GRVIMGSEVG VVDVPPQDVS KKGRLNPGMM LLVDFENHAV VDDDALKKEY STRQPYAEWL
QHQKILLKDI VDSVSEDCTS PRIIGTLQDL QPKKTDATRD NMGIHGLVPP LKAFGYTVEA
LEMLLLPMAK DGVEALGSMG NDAPLAVMTD RPKLSFEYFK QMFAQVTNPP IDPIREAIVT
STECMIGPEG DLTESTEEQF HRLSLKGPLI SPLEMEALKK MNYQGWRSKI IDITFPREEG
PTGLEKALDR ICVEARKAIS KGFKMLVLSD RGTSPERVPV SSLLAVGTVH HHLVSTLERT
RIGLVVESGE PREVHHFCTL LGFGADAICP YLAVEAIWRL QVDGKIPSKE NGVLSSKDEL
VQKYFKASNS GILKVLAKMG ISTLASYKGA QIFEALGLSS DVVQRCFRGT PSRVEGATFE
MLAKDSLRLH ELAFPSRKLP PGSAEAHALP NPGDYHWRKD GEIHLNDPLA MAKLQEAART
NSVGAYKDYS KRIYELNKKC SLRGMLKFKA SKTPVALEEV EPASEIVKRF CTGAMSYGSI
SLEAHTTLAM AMNQIGGKSN TGEGGENPSR LEALPNGQMN PKRSAIKQVA SGRFGVTSYY
LTNADELQIK MAQGAKPGEG GELPGHKVIG DIATTRNSTS GVGLISPPPH HDIYSIEDLA
QLIYDLKNSN PGARISVKLV SEAGIGVVAS GVVKGHADHV LISGHEGGTG ASRWTGIKNA
GLPWELGLAE THQTLVANDL RGRTTLQTDG QLKTGRDINT CPVGIATQDP VLREMFAGEP
EDVINFFFMV AEEARELMAE MGFRTMDEMV GRADMLEVYK SVTASNEKLK NIDLSLLLRP
AADIRPDAAQ RCVQKQDHNL GMALDQQLIK VSKHALENGY PVYLESPVVN VNRAVGTMLS
HEVTKKYKME GLPADTIHVK LTGNAGQSLG AFLCRGITLE LEGDSNDYVG KGLCGGRVVV
YPPRDSGFDP KENIVIGNVA LYGATSGEAY FNGMAAERFC VRNSGAKAVV EGVGDHGCEY
MTGGTVVILG KTGKNFAAGM SGGIAYVYDV DGKFRLRCNP GQVDLEDVLE DEDVLTLRAM
IQQHQRHTKS QHAKQILDEF DSALPKFVKV FPRDYKRALN EEKAKKRAAE EEEARLATVD
AFQELKKMAE AATNGGAAAV AETPAKARPT IIPDAVKHRG FISYERETLP YRPAQNDDLL
KTQSARCMDC GTPFCNQDSS GCPLGNKIPE WNELVHQGRW REALDRLLET NNFPEFTGRV
CPAPCEGACV LGIISIKTME CTIIDKAFEE GWMVPRPPAY RTGKRVAIVG SGPAGLAAAD
QLNKAGHSVT VFERADRIGG LMMYGVPNMK TDKVEVVQRR VNLMAAEGIE FIVNANVGVD
KLFSVERLMS DYDSLLLACG ATKPRDLKVE GREYEGIHFA MEFLHANTKS LLDSGLKDNN
YISAKDKKVV VIGGGDTGTD CIGTAVRHGC KSVVNLELLP QPPATRAPGN PWPQWPRIFR
VDYGHAEAKE KFGSDPRSYE VTTKKFITDG DNRVSGLVLK RVRWFKDASG RFQREEIEGS
EEIIEADLVL LAMGFVGPEQ DVAEKLKVAT NDAATTFKAE YGKFATNVKG VFAAGDCRRG
QSLVVWAIAE GRQAAAQIDK FLMEDTSKVG EELKAARKKM GMLI
//
